Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods

Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by...

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Main Authors: Ruichen Zhao, Xiaoli Qin, Jinfeng Zhong
Format: Article
Language:English
Published: MDPI AG 2021-08-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/26/16/5092
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spelling doaj-8930c0f63b6649708b5b4d360b4ba46f2021-08-26T14:08:23ZengMDPI AGMolecules1420-30492021-08-01265092509210.3390/molecules26165092Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation MethodsRuichen Zhao0Xiaoli Qin1Jinfeng Zhong2College of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaEffect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 10<sup>4</sup> L/mol (298 K), 6.17 × 10<sup>4</sup> L/mol (305 K) and 5.73 × 10<sup>4</sup> L/mol (312 K) at pH 2.0, which was greater than that (3.98 × 10<sup>4</sup> L/mol at 298 K, 3.90 × 10<sup>4</sup> L/mol at 305 K and 3.41 × 10<sup>4</sup> L/mol at 312 K) at pH 7.4. Molecular docking study showed that binding energy of β-casein-curcumin complex at pH 2.0 (−7.53 kcal/mol) was lower than that at pH 7.4 (−7.01 kcal/mol). The molecular dynamics simulation study showed that the binding energy (−131.07 kJ/mol) of β-casein-curcumin complex was relatively low at pH 2.0 and 298 K. α-Helix content in β-casein was decreased and random coil content was increased in the presence of curcumin. These results can promote a deep understanding of interaction between curcumin and β-casein and provide a reference for improving the bioavailability of curcumin.https://www.mdpi.com/1420-3049/26/16/5092hydrophobic interactionfluorescence quenchingmolecular dockingsecondary structure contentthermodynamic parameters
collection DOAJ
language English
format Article
sources DOAJ
author Ruichen Zhao
Xiaoli Qin
Jinfeng Zhong
spellingShingle Ruichen Zhao
Xiaoli Qin
Jinfeng Zhong
Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods
Molecules
hydrophobic interaction
fluorescence quenching
molecular docking
secondary structure content
thermodynamic parameters
author_facet Ruichen Zhao
Xiaoli Qin
Jinfeng Zhong
author_sort Ruichen Zhao
title Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods
title_short Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods
title_full Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods
title_fullStr Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods
title_full_unstemmed Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods
title_sort interaction between curcumin and β-casein: multi-spectroscopic and molecular dynamics simulation methods
publisher MDPI AG
series Molecules
issn 1420-3049
publishDate 2021-08-01
description Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 10<sup>4</sup> L/mol (298 K), 6.17 × 10<sup>4</sup> L/mol (305 K) and 5.73 × 10<sup>4</sup> L/mol (312 K) at pH 2.0, which was greater than that (3.98 × 10<sup>4</sup> L/mol at 298 K, 3.90 × 10<sup>4</sup> L/mol at 305 K and 3.41 × 10<sup>4</sup> L/mol at 312 K) at pH 7.4. Molecular docking study showed that binding energy of β-casein-curcumin complex at pH 2.0 (−7.53 kcal/mol) was lower than that at pH 7.4 (−7.01 kcal/mol). The molecular dynamics simulation study showed that the binding energy (−131.07 kJ/mol) of β-casein-curcumin complex was relatively low at pH 2.0 and 298 K. α-Helix content in β-casein was decreased and random coil content was increased in the presence of curcumin. These results can promote a deep understanding of interaction between curcumin and β-casein and provide a reference for improving the bioavailability of curcumin.
topic hydrophobic interaction
fluorescence quenching
molecular docking
secondary structure content
thermodynamic parameters
url https://www.mdpi.com/1420-3049/26/16/5092
work_keys_str_mv AT ruichenzhao interactionbetweencurcuminandbcaseinmultispectroscopicandmoleculardynamicssimulationmethods
AT xiaoliqin interactionbetweencurcuminandbcaseinmultispectroscopicandmoleculardynamicssimulationmethods
AT jinfengzhong interactionbetweencurcuminandbcaseinmultispectroscopicandmoleculardynamicssimulationmethods
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